The nucle(ol)ar Tif6p and Efl1p are required for a late cytoplasmic step of ribosome synthesis.

Abstract:

:Deletion of elongation factor-like 1 (Efl1p), a cytoplasmic GTPase homologous to the ribosomal translocases EF-G/EF-2, results in nucle(ol)ar pre-rRNA processing and pre-60S subunits export defects. Efl1p interacts genetically with Tif6p, a nucle(ol)ar protein stably associated with pre-60S subunits and required for their synthesis and nuclear exit. In the absence of Efl1p, 50% of Tif6p is relocated to the cytoplasm. In vitro, the GTPase activity of Efl1p is stimulated by 60S, and Efl1p promotes the dissociation of Tif6p-60S complexes. We propose that Tif6p binds to the pre-60S subunits in the nucle(ol)us and escorts them to the cytoplasm where the GTPase activity of Efl1p triggers a late structural rearrangement, which facilitates the release of Tif6p and its recycling to the nucle(ol)us.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Senger B,Lafontaine DL,Graindorge JS,Gadal O,Camasses A,Sanni A,Garnier JM,Breitenbach M,Hurt E,Fasiolo F

doi

10.1016/s1097-2765(01)00403-8

subject

Has Abstract

pub_date

2001-12-01 00:00:00

pages

1363-73

issue

6

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(01)00403-8

journal_volume

8

pub_type

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